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PubMed1983

The distribution of cholinesterase and cytochrome oxidase within the dorsal lateral geniculate nucleus of the squirrel monkey.

Within the dorsal lateral geniculate nucleus (dLGN) of the squirrel monkey, acetylcholinesterase (AChE) and cytochrome oxidase (CO) are distributed preferentially in the magnocellular layers. Butyrylcholinesterase (BuChE) activity is comparatively weak, but higher in the parvocellular than in the magnocellular layers. The different patterns of distribution of AChE within the dLGN in different primate species signify differences in geniculate organization, which may reflect adaptation to different visual habitats.

Acetylcholinesterase↗
PubMed1984

Reaction of caa3-type terminal cytochrome oxidase from the thermophilic bacterium PS3 with oxygen and carbon monoxide at low temperatures.

Reaction of O2 and CO with a caa3-type terminal cytochrome oxidase (EC 1.9.3.1) from the thermophilic bacterium PS3 grown with high aeration was studied at low temperatures. The CO recombination at the temperature range studied (-50 degrees C to -80 degrees C) followed first-order kinetics with an activation energy of 29.3 kJ/mol (7.0 kcal/mol). In the presence of O2 at -113 degrees C the photolysed reduced form binds O2 to form an 'oxy' intermediate similar to Compound A. At a higher temperature (-97 degrees C) another intermediate, similar to Compound B, is formed as a result of electron transfer from the enzyme to the liganded O2.

Carbon Monoxide↗
PubMed2000

The activity of cytochrome oxidase is increased in circulating lymphocytes of patients with chronic obstructive pulmonary disease, asthma, and chronic arthritis.

We have previously shown that the activity of cytochrome oxidase (CytOx) in skeletal muscle of patients with chronic obstructive pulmonary disease (COPD) was higher than in healthy control subjects. The mechanisms and implications of this observation were unclear. In particular, it was not known if this abnormality can occur also in: (1) cell types other than muscle cells, and (2) other chronic inflammatory diseases. To obtain further insight into these questions, we measured the activity of CytOx in circulating lymphocytes in patients with stable COPD (n = 17), bronchial asthma (n = 6), or chronic arthritis (n = 5), and in healthy control subjects (n = 8). We found that, compared with healthy subjects (280 +/- 117 nKat/microg protein), patients with COPD showed increased CytOx activity (430 +/- 150 nKat/microg protein, p = 0.01) in lymphocytes. Further, this activity was negatively related to the degree of airflow obstruction present in these patients (r = -0.53, p < 0.05). We also found that the activity of CytOx in circulating lymphocytes was higher than normal in patients with chronic arthritis (411 +/- 130 nKat/microg protein, p < 0.05) and, particularly, in patients with bronchial asthma (1,667 +/- 1,027 nKat/microg protein, p < 0.001). These results show that the increased CytOx activity previously reported in skeletal muscle of patients with COPD is also detected in other cell types (such as circulating lymphocytes) and in other chronic inflammatory diseases (such as bronchial asthma and chronic arthritis). The mechanisms and implications of these findings deserve further investigation.

Arthritis↗
PubMedDate not supplied

Cytochrome-oxidase and succinate dehydrogenase activity in the rat kidney preserved by cold storage, correlated with the study of mitochondrial suspension.

Succinate dehydrogenase (SDH) and cytochrome-oxidase (CO) activities were determined biochemically in the white rat kidneys after 24, 48, 72 hours preservation by cold storage. The investigations also included the study of infrastructural alterations in mitochondrial suspensions, separately for the medulla and the cortex. The comparison of the enzymatic activity curves showed a mirror-like aspect with a maximum at 24 hours for CO and a minimum for SDH, and a constantly more intense activity in the medulla.

Animals↗
PubMed2000

Phylogenetic relationships among bumble bees (Bombus, latreille) inferred from mitochondrial cytochrome b and cytochrome oxidase I sequences.

We conducted a molecular study intending to derive an estimate of the relationships within the genus Bombus (bumble bees) by comparing the mitochondrial cytochrome b and cytochrome oxidase I (COI) genes from 19 species, spanning 10 of approximately 16 European subgenera and 3 subgenera from North and South America. Our trees differ from the most recent classifications of bumble bees. Although bootstrap values for deep branches are low, our sequences show significant data structure and low homoplasy, and all trees share some groups and patterns. In all cases, the subgenus Bombus s. str. clusters among the most derived bumble bees, contrary to other molecular studies. In all trees, B. funebris is the sister taxon of B. robustus, and in five of the six trees, B. wurflenii is the sister taxon to this clade. B. nevadensis is basal to the other species in the analysis of the cytochrome b gene, but appears to be among the most derived according to the analysis of the COI region. The species representing the subgenera Thoracobombus and Fervidobombus are consistently among the earliest diverged. Species that appear in very different positions in different trees are B. nevadensis, B. mesomelas, B. balteatus, and B. hyperboreus. All subgenera with two representatives in our analysis are apparently monophyletic except Fervidobombus, Melanobombus, and Pyrobombus. The groups formed by pocket makers and non-pocket makers within Bombus also appear to be paraphyletic, and therefore some subgenera may not accurately reflect phylogeny.

Animals↗
PubMed1978

Microspectrophotometric quantitation of the diaminobenzidine reaction for histochemical demonstration of cytochrome oxidase activity.

Polyacrylamide models in which an extract of cattle heart mitochondria was incorporated, as well as cryostat sections of tongue muscle and epithelium, were used to set up the conditions under which the histochemical reaction for the demonstration of cytochrome oxidase can be quantitated. Using diaminobenzidine in a concentration of 5.5 mM, cytochrome C in a fixed concentration of 76 micron and keeping the incubation medium away from direct light action, enzyme activity can be evaluated by means of direct microphotometry on tissue sections. Each biologic model requires previous individual determination of the measurement limits. These limits can be readily established by using a small chamber for the incubation medium, which can be placed in the microphotometer, allowing the reaction rate to be following using a single section.

3,3'-Diaminobenzidine↗
PubMed1981

Quaternary structure of bovine cytochrome oxidase.

A hydrodynamically homogeneous preparation of bovine mitochondrial cytochrome c oxidase can be obtained by anion-exchange chromatography of alkaline-treated enzyme, followed by a gel permeation chromatography step, which further removes some (aggregated) apoprotein. The molecular weight, Mr, of the monodisperse enzyme in Triton X-100 was found to be 210000. This complex is composed of six different polypeptides, with Mr summing up to about 110000 in toto, in a relative one-to-one stoichiometry. Two sets of these subunits constitute the 210000-Mr enzyme complex. In contrast to our earlier report [Saraste, Penttilä, Coggins, and Wikström, FEBS Lett. 114 (1980) 35-38] the 210000-Mr enzyme contains four (and not two) haems A, and therefore represents the dimer of cytochrome aa3. One of the proposed seven subunits, number III, is lacking in this enzyme preparation.

Animals↗
PubMed1994

Kinetics of ligand binding of cytochrome oxidases: a comparative study.

The plethora of microbial oxidases revealed by photochemical action spectra (Chance, B. (1989)) Biochim. Biophys. Acta 1000, 345-347) has led to detailed identification, purification and overproduction in many species, to the point where kinetic comparison of properties seems to allow structure/function deductions. This work compares the carbon monoxide recombination of five types of oxidases obtained from various organisms. The results are plotted in an Arrhenius-type plot and suggest that the carbon monoxide ligation is a sensitive indicator of the heme environment specific for an oxidase expressed under a given oxygen concentration. This survey of the carbon monoxide recombination kinetics of naturally occurring cytochrome oxidases in whole cells shows evidence for structural control of the reaction kinetics.

Animals↗
PubMed2004

Regional brain variations of cytochrome oxidase activity in spontaneously hypertensive mice.

To explore the central disturbances resulting from blood pressure changes, spontaneously hypertensive mice (SHM) were compared to normotensive controls for cytochrome oxidase (CO) activity, an index of oxidative capacity in the central nervous system and a marker of long-term regional brain metabolism and neuronal activity. In all brain areas presenting significant enzymatic variations, only increases in CO activity were found in SHM, particularly the central autonomic network. However, only specific regions were affected, namely the insular cortex and the hypothalamic nuclei principally involved in high-order autonomic control. Altered limbic structures included the lateral septum, various hippocampal subregions, as well as prelimbic cortex. CO activity was also elevated in several forebrain regions, including those directly connected to the limbic system, such as the nucleus accumbens, the claustrum, and dorsomedial and reticular thalamic nuclei, as well as subthalamic and ventrolateral thalamic nuclei. In the brainstem, the only regions affected were the locus coeruleus, site of noradrenergic cell bodies, the trigeminal system, and four interconnected regions: the inferior colliculus, the paramedial reticular formation, the medial vestibular, and the cerebellar fastigial nuclei. These data show that specific regions modulating sympathetic nerve discharge are activated in young adult SHM, possibly due to mitochondrial dysfunction and excitotoxicity.

Animals↗
PubMed2002

[Effects of hypoxic exposure on coordinative expression of cytochrome oxidase subunits I and IV in rat cerebral cortex].

This study was intended to evaluate the effects of hypoxic exposure on gene expression and coordination of cytochrome oxidase (COX) subunits I (COX I) and IV (COX IV) encoded by mtDNA and nDNA respectively in rat cerebral cortex. Male Wistar rats were exposed to hypoxia in a hypobaric chamber simulating high altitude at 5000 m for 2, 5, 15 and 30 d. Control rats were fed outside the hypobaric chamber (the height was 300 m above sea level). Rats were sacrificed and mitochondria from cerebral cortex were isolated by differential centrifugation at each time point. COX I and COX IV proteins in isolated rat cerebral cortex mitochondria were detected by Western blot analysis and mRNA in the cerebral cortex by RT-PCR. The ratios of protein and mRNA were used to estimate the coordinative expression of two subunits. The results showed that COX I mRNA increased significantly at 2 and 5 d, and decreased to the control level at 15 and 30 d; COX IV mRNA remarkably increased at 2, 5 and 15 d, and dropped below the control level at 30 d. The mRNA ratio of COX IV to COX I reached a peak at 15 d, but showed no differences between other time points. The Western blot analysis of COX I and COX IV in isolated rat cerebral cortex mitochondria showed no obvious changes during hypoxic exposure. Our findings demonstrate that hypoxia can affect mRNA expression of COX I and COX IV and their coordination, while protein expression of both subunits are stable and coordinative. This study suggests that the expression of COX I and COX IV proteins during hypoxic exposure is coordinately regulated by post-transcriptional mechanisms.

Animals↗
PubMed2001

Mammalian subunit IV isoforms of cytochrome c oxidase.

Cytochrome c oxidase (COX) contains ten nuclear encoded subunits, three of them known to show tissue isoforms in mammals. We have now found a fourth isoform, for subunit IV, in human, rat and mouse (COX IV-2). Comparison of the two human isoform genes shows a similar structural organization, including an overall size of about 8 kb, the presence of five exons, and the initiation of translation in the second exon, consistent with formation by gene duplication. Also consistent is the higher identity of precursor peptides of 78% within the new IV-2 isoform (average in the three species) compared to 44% average identity with the IV-1 isoform. Northern analysis and quantitative PCR with human and rat tissues show high IV-2 expression in adult lung and lower expression in all other tissues investigated, including fetal lung. In contrast, the IV-1 isoform is ubiquitously expressed. In situ hybridizations were performed to localize isoform transcripts in rat lung. Both isoforms are found in similar ratios in most lung cell types except for smooth muscle and respiratory epithelium, which have a IV-2 and a IV-1 preference, respectively. Structural modeling of the IV-2 isoform from human, based on the bovine crystal data, produces a conformation in which two of three conserved cysteine groups, exclusively present in the mammalian IV-2 isoform, are in close proximity. The formation of a cysteine bond and the implications for function of these sequence differences for subunit IV, which plays a pivotal role in COX regulation, are discussed.

Amino Acid Sequence↗
PubMed1984

Local cytochrome oxidase activity in the cerebral cortex of the rat, histochemically detected with the DAB-method: a micro-densitometric and electron microscope study.

For demonstration of the local cytochrome oxidase activity, coronal sections through the frontal cortex of four Sprague-Dawley rats were incubated with DAB medium after Seligman et al. (1968). The pattern of distribution of the DAB reaction product (DAB-RP) was measured at a wavelength of 460 nm. Cryostat sections were scanned with a microdensitometer. The cytochrome reaction product was accumulated in the laminae I and IV. A comparative morphometric study of mitochondrial profiles in ultra-thin sections through equivalent cortical regions showed an approximately similar distribution in percentage of areal density of the mitochondria labeled by DAB-RP. On average 30% of the mitochondrial profiles were labeled with DAB-RP which was localized in the intracristate spaces and the outer mitochondrial compartment. The marked mitochondria mainly occurred in dendrites. Furthermore, the mean and median value of the size distribution of marked mitochondrial profiles was shifted to greater values when compared with non-marked ones.

3,3'-Diaminobenzidine↗
PubMed2005

Evidence for the association of yeast mitochondrial ribosomes with Cox11p, a protein required for the Cu(B) site formation of cytochrome c oxidase.

Cytochrome c oxidase is the terminal enzyme of the mitochondrial (mt) respiratory chain. It contains copper ions, which are organized in two centres, Cu(A) and Cu(B). The Cu(A) site of subunit Cox2p is exposed to the mt intermembrane space, while the Cu(B) site of subunit Cox1p is buried in the inner mt membrane. Incorporation of copper into the two centres is crucial for the assembly and activity of the enzyme. Formation of the Cu(B) site is dependent on Cox11p, a copper-binding protein of the mt inner membrane. Here, we experimentally prove that Cox11p possesses a N(in)-C(out) topology, with the C-terminal copper-binding domain exposed in the mt intermembrane space. Furthermore, we provide evidence for the association of Cox11p with the mt translation machinery. We propose a model in which the Cu(B) site is co-translationally formed by a transient interaction between Cox11p and the nascent Cox1p in the intermembrane space.

Base Sequence↗
PubMed1993

An improved staining technique for cytochrome C oxidase.

Cytochrome C oxidase (CO) has been shown to be an indicator of neuronal activity in the brain. In the primate visual cortex, CO staining also differentiates cell populations encoding visual properties such as color, contrast, ocularity, and movement. We have developed a modified method which dramatically enhances the intensity and contrast of CO staining. This method can be applied to both fixed and non-fixed tissues. The sensitivity of this method is sufficiently high that, even after years of storage, tissues can still be well stained for CO activity. Such tissue is poorly stained with current methods. This CO staining technique may also be useful for double labeling of CO with other anatomical markers.

Animals↗
PubMed2006

Combined DFT and electrostatics study of the proton pumping mechanism in cytochrome c oxidase.

Cytochrome c oxidase is a redox-driven proton pump which converts atmospheric oxygen to water and couples the oxygen reduction reaction to the creation of a membrane proton gradient. The structure of the enzyme has been solved; however, the mechanism of proton pumping is still poorly understood. Recent calculations from this group indicate that one of the histidine ligands of enzyme's CuB center, His291, may play the role of the pumping element. In this paper, we report on the results of calculations that combined first principles DFT and continuum electrostatics to evaluate the energetics of the key energy generating step of the model-the transfer of the chemical proton to the binuclear center of the enzyme, where the hydroxyl group is converted to water, and the concerted expulsion of the proton from delta-nitrogen of His291 ligand of CuB center. We show that the energy generated in this step is sufficient to push a proton against an electrochemical membrane gradient of about 200 mV. We have also re-calculated the pKa of His291 for an extended model in which the whole Fe(a3)-CuB center with their ligands is treated by DFT. Two different DFT functionals (B3LYP and PBE0), and various dielectric models of the protein have been used in an attempt to estimate potential errors of the calculations. Although current methods of calculations do not allow unambiguous predictions of energetics in proteins within few pKa units, as required in this case, the present calculation provides further support for the proposed His291 model of CcO pump and makes a specific prediction that could be targeted in the experimental test.

Electron Transport Complex IV↗
PubMed2006

Inhibition of proton pumping by zinc ions during specific reaction steps in cytochrome c oxidase.

Cytochrome c oxidase (CytcO) is a redox-driven proton pump in the respiratory chain of mitochondria and many aerobic bacteria. The results from several studies have shown that zinc ions interfere with both the uptake and release of protons, presumably by binding near the orifice of the proton entrance and exit pathways. To elucidate the effect of Zn2+ binding on individual electron and proton-transfer reactions, in this study, we have investigated the reaction of the fully reduced R. sphaeroides CytcO with O2, both with enzyme in detergent solution and reconstituted in phospholipid vesicles, and, with and without, Zn2+. The results show that addition of Zn2+ at concentrations of < or = 250 microM to the outside of the vesicles did not alter the transition rates between intermediates PR (P3)-->F3-->O4. However, proton pumping was impaired specifically during the P3-->F3, but not during the F3-->O4 transition at Zn2+ concentrations of < or = 25 microM. Furthermore, proton pumping during the P3-->F3 transition was typically impaired with the "as isolated" CytcO, which was found to contain Zn2+ ions at microM concentration. As has already been shown, Zn2+ was also found to obstruct proton uptake during the P3-->F3 transition, presumably by binding to a site near the orifice of the D-pathway. In this work we found a KI of approximately 1 microM for this binding site. In conclusion, the results show that Zn2+ ions bind on both sides of CytcO and that binding of Zn2+ at the proton output side selectively impairs proton release during the P3-->F3 transition.

Biological Transport↗
PubMed2006

The K-pathway revisited: a computational study on cytochrome c oxidase.

Cytochrome c oxidase contains two established proton-conducting structures, the D- and K-pathways. The role of the K-pathway appears to be to conduct the first two protons to be used in water formation, which are taken up on reduction of the oxidized enzyme. Previous computational work has suggested that Lys(I)-319 is neutral over a large pH range and in various redox states. We have constructed oxidase models in different redox states using quantum-chemically derived charge parameters for the redox metal centers. The protonation behaviour of titratable sites in the two-subunit enzyme was defined by continuum electrostatics. The calculations reported here show substantial protonation of Lys(I)-319 at neutral pH once the stable X-ray crystallographic water molecule found immediately next to it is treated explicitly. The immediate structure of the Lys(I)-319 environment is independent of redox state, but the pK(a) value of this residue changes with the redox state of the binuclear heme a3/Cu(B) site whenever that change is electrically uncompensated. Lys(I)-319 is also found to interact electrostatically with the conserved residue Glu(II)-62 in subunit II. These results are discussed in relation to the role of the K-pathway in oxidase function.

Animals↗